ID   SSUB1_RHOJR             Reviewed;         245 AA.
AC   Q0SK28;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Aliphatic sulfonates import ATP-binding protein SsuB 1 {ECO:0000255|HAMAP-Rule:MF_01724};
DE            EC=7.6.2.14 {ECO:0000255|HAMAP-Rule:MF_01724};
GN   Name=ssuB1 {ECO:0000255|HAMAP-Rule:MF_01724};
GN   OrderedLocusNames=RHA1_ro00272;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex SsuABC involved in
CC       aliphatic sulfonates import. Responsible for energy coupling to the
CC       transport system. {ECO:0000255|HAMAP-Rule:MF_01724}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + aliphatic sulfonate-[sulfonate-binding
CC         protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 +
CC         [sulfonate-binding protein]Side 1.; EC=7.6.2.14;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01724};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (SsuB),
CC       two transmembrane proteins (SsuC) and a solute-binding protein (SsuA).
CC       {ECO:0000255|HAMAP-Rule:MF_01724}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01724};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01724}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Aliphatic
CC       sulfonates importer (TC 3.A.1.17.2) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01724}.
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DR   EMBL; CP000431; ABG92108.1; -; Genomic_DNA.
DR   RefSeq; WP_011593561.1; NC_008268.1.
DR   AlphaFoldDB; Q0SK28; -.
DR   SMR; Q0SK28; -.
DR   STRING; 101510.RHA1_ro00272; -.
DR   EnsemblBacteria; ABG92108; ABG92108; RHA1_ro00272.
DR   KEGG; rha:RHA1_ro00272; -.
DR   PATRIC; fig|101510.16.peg.300; -.
DR   eggNOG; COG1116; Bacteria.
DR   HOGENOM; CLU_000604_1_22_11; -.
DR   OMA; FAFMPQR; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51291; SSUB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..245
FT                   /note="Aliphatic sulfonates import ATP-binding protein SsuB
FT                   1"
FT                   /id="PRO_0000279954"
FT   DOMAIN          9..227
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ   SEQUENCE   245 AA;  27043 MW;  757F9744AA41AA5C CRC64;
     MPATNLVGLD LVGIGHRYRD TTVLHDIDLT VEPGEFVSFL GPSGVGKSTL LRIIAGLEQP
     THGVVESTGG TSGGTMSRMM FQEDRLLPWR NVLDNVQLGT RHQRERALEL LYDVGLAGRE
     KDWPSELSGG QRQRVALARA LLHQPDVLLL DEPFGALDAI TRVAMQQLLE RVLAEQPRTV
     LLVTHDVEEA LVLSDRVLLL TDQGITRDLR IPHARPRHRG DAQLAAWKEE LLDGLLQADN
     ALSSL